ID Q0SCE8_RHOJR Unreviewed; 528 AA.
AC Q0SCE8;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=acetolactate synthase {ECO:0000256|ARBA:ARBA00013145};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145};
GN OrderedLocusNames=RHA1_ro02985 {ECO:0000313|EMBL:ABG94788.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG94788.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
RN [2] {ECO:0007829|PDB:7ORX}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH THIAMINE
RP DIPHOSPHATE.
RX PubMed=30946572; DOI=10.1021/acs.biochem.9b00177;
RA Wei Z., Wilkinson R.C., Rashid G.M.M., Brown D., Fulop V., Bugg T.D.H.;
RT "Characterization of Thiamine Diphosphate-Dependent 4-Hydroxybenzoylformate
RT Decarboxylase Enzymes from <i>Rhodococcus jostii</i> RHA1 and
RT <i>Pseudomonas fluorescens</i> Pf-5 Involved in Degradation of Aryl
RT C<sub>2</sub> Lignin Degradation Fragments.";
RL Biochemistry 58:5281-5293(2019).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2;
CC Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000673};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004974}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP000431; ABG94788.1; -; Genomic_DNA.
DR RefSeq; WP_011595658.1; NC_008268.1.
DR PDB; 7ORX; X-ray; 2.60 A; AAA/BBB/CCC/DDD=1-528.
DR AlphaFoldDB; Q0SCE8; -.
DR SMR; Q0SCE8; -.
DR KEGG; rha:RHA1_ro02985; -.
DR PATRIC; fig|101510.16.peg.3014; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_11; -.
DR OrthoDB; 2443624at2; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000008710; Chromosome.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:RHEA.
DR GO; GO:0050695; F:benzoylformate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02002; TPP_BFDC; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF133; BENZOYLFORMATE DECARBOXYLASE; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:7ORX};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Lyase {ECO:0000313|EMBL:ABG94788.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008710};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..114
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 190..323
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..521
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 26
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0007829|PDB:7ORX"
FT BINDING 377
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0007829|PDB:7ORX"
FT BINDING 378
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0007829|PDB:7ORX"
FT BINDING 401
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0007829|PDB:7ORX"
FT BINDING 403
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0007829|PDB:7ORX"
FT BINDING 429
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0007829|PDB:7ORX"
FT BINDING 430
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0007829|PDB:7ORX"
FT BINDING 455
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0007829|PDB:7ORX"
FT BINDING 459
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0007829|PDB:7ORX"
FT BINDING 460
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0007829|PDB:7ORX"
SQ SEQUENCE 528 AA; 55072 MW; A0730651B91954E0 CRC64;
MATVSEVTYE LLRARGLTTV FGNPGSNELP FLSGMPDDFR YVLGLHEGAV LSMADGYSLV
TGEATLVNLH AASGSGNAMG ALTNSVYSHS PLVVTAGQQV RSTIGQEVML SNVDAGTLMK
PLVKWSSEPT CAEDVPRTIN QAIHTALLPA KGPVYVSVPY DDWAAEAPPE SAGLLAREVH
SAASLSGDQI NDLIETLESA TNPVLVLGPA VDADRANADA VLLAEKLRAP VWIAPSPSRC
PFPTRHPSFR GVLPAGVADL SKTLEGHDLI LVVGAPVFRY HQYVPGNYLP GGARLIHVTD
DGGEAARAPI GEAYVAPVGS TLEILANMVK PSDRSPLPPL GDFEEAVSVG AGLDPAQLFA
LVRAGAPDDA IYVNESTSTS DAFWSQMDLS HQGSYYFPAS GGLGFGLPAA VGAQLASPDR
QVIGLIGDGS ANYGITALWS AAQYKIPVVI IILNNGTYGA LRGFSKILNT GETPGLDVPG
IDFVHLAEGY GVRGTAVATA EDFTTAFKSA LAADAPTLIE VRTNFDES
//
